coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  62 HGDSVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQ 141
Cdd:cd20482    1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755503761 142 KAQLEQLLADMRTGVEFTEHLLTSGSDLEILITKGVVVERLR 183
Cdd:cd20482   81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARLQ 122

B-box-type 2 zinc finger found in tripartite motif-containing protein 45 (TRIM45) and similar proteins; TRIM45, also known as RING finger protein 99 (RNF99), is a novel receptor for activated C-kinase (RACK1)-interacting protein that suppresses transcriptional activities of Elk-1 and AP-1 and downregulates mitogen-activated protein kinase (MAPK) signal transduction by inhibiting RACK1/PKC (protein kinase C) complex formation. It also negatively regulates tumor necrosis factor alpha (TNFalpha)-induced nuclear factor-kappaB (NF-kappa B)-mediated transcription and suppresses cell proliferation. TRIM45 belongs to the C-X subclass of TRIM (tripartite motif) family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a filamin-type immunoglobulin (IG-FLMN) domain and NHL repeats positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 755503761  16 PILCPSHPAEELRLFCELCDRPVCRDCVVGEHREHPYDFTSNV 58
Cdd:cd19785    1 PVLCPFHPAEELRLFCETCDKPVCRDCVLVEHRGHQCDFTSDV 43

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  62 HGDSVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQ 141
Cdd:cd20482    1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755503761 142 KAQLEQLLADMRTGVEFTEHLLTSGSDLEILITKGVVVERLR 183
Cdd:cd20482   81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARLQ 122

Filamin/ABP280 repeat;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  225 VDPAQCVLQGEDLHRAREKQTASFTLFCKDASGqsmgrggdNVHVEVVpkDKKDSPIRTVVQDNKDGSYRVSYTPKEPGI 304
Cdd:pfam00630   2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG--------EGEVEVT--GPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                          90
                  ....*....|....*..
gi 755503761  305 YTVWVCIREQHVQGSPF 321
Cdd:pfam00630  72 YTVSVKFNGQHIPGSPF 88

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761    65 SVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQKAQ 144
Cdd:smart00502   4 ALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQLES 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 755503761   145 LEQLLADMRTGVEFTEHLLTSGSDLEILITKGVVVERLRKL 185
Cdd:smart00502  84 LTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNL 124

B-Box-type zinc finger;

                           10        20        30
                   ....*....|....*....|....*....|....*
gi 755503761    18 LCPSHPAEELRLFCELCDRPVCRDCVVGEHREHPY 52
Cdd:smart00336   5 KCDSHGDEPAEFFCEECGALLCRTCDEAEHRGHTV 39

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761   53 DFTSNVIHKHGDSVRELLRDTQPHVEALEDALAQ-IKsvnnALQERVEAVAADVRTFSEGYIKAIEEH--------RDKL 123
Cdd:pfam01442  55 PYLEELQAKLGQNVEELRQRLEPYTEELRKRLNAdAE----ELQEKLAPYGEELRERLEQNVDALRARlapyaeelRQKL 130

                          90       100       110
                  ....*....|....*....|....*....|....
gi 755503761  124 LQQLDDIRIQRETALQLQKAQLEQLLADMRTGVE 157
Cdd:pfam01442 131 AERLEELKESLAPYAEEVQAQLSQRLQELREKLE 164

coiled-coil (CC) domain of Drosophila brain tumor (brat) and similar proteins; This family contains the coiled-coil (CC) region of Drosophila brain tumor (Brat), a translational repressor that belongs to the tripartite motif (TRIM) protein superfamily. TRIM proteins play important roles in various cellular processes and are involved in many diseases which consists of two B-box domains and a coiled-coil (CC) domain at the N-terminal region, and an NHL domain at the C-terminus. Brat localizes at the basal cortex during asymmetric division of Drosophila neuroblasts by directly interacting with the scaffolding protein Miranda (Mira), which it does through the CC-NHL domain tandem, indicating that the function of the Brat CC domain is to assemble Brat-NHL in dimeric form which is necessary for Mira binding. Brat CC forms an elongated antiparallel dimer similar to its other TRIM protein counterparts, but the overall length of Brat CC dimer is shorter than the TRIMs.

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  62 HGDSVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQ 141
Cdd:cd20482    1 HKESLQQLLEEARAKIPELRDALKNVEHALSRLQMQYHKAQNEINETFQFYRSMLEERKDELLKELESIYNAKQLSLNEQ 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 755503761 142 KAQLEQLLADMRTGVEFTEHLLTSGSDLEILITKGVVVERLR 183
Cdd:cd20482   81 QQKLQETIEKIQQGCEFTERLLKHGSETEVLLFKKLLEARLQ 122

Filamin/ABP280 repeat;

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  225 VDPAQCVLQGEDLHRAREKQTASFTLFCKDASGqsmgrggdNVHVEVVpkDKKDSPIRTVVQDNKDGSYRVSYTPKEPGI 304
Cdd:pfam00630   2 ADASKVKASGPGLEPGVVGKPAEFTVDTRDAGG--------EGEVEVT--GPDGSPVPVEVTDNGDGTYTVSYTPTEPGD 71

                          90
                  ....*....|....*..
gi 755503761  305 YTVWVCIREQHVQGSPF 321
Cdd:pfam00630  72 YTVSVKFNGQHIPGSPF 88

B-Box C-terminal domain; Coiled coil region C-terminal to (some) B-Box domains

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761    65 SVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGYIKAIEEHRDKLLQQLDDIRIQRETALQLQKAQ 144
Cdd:smart00502   4 ALEELLTKLRKKAAELEDALKQLISIIQEVEENAADVEAQIKAAFDELRNALNKRKKQLLEDLEEQKENKLKVLEQQLES 83

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 755503761   145 LEQLLADMRTGVEFTEHLLTSGSDLEILITKGVVVERLRKL 185
Cdd:smart00502  84 LTQKQEKLSHAINFTEEALNSGDPTELLLSKKLIIERLQNL 124

B-box-type 2 zinc finger found in transcription intermediary factor 1 (TIF1) family; This family corresponds to the TIF1 family of transcriptional cofactors including TIF1-alpha (TRIM24), TIF1-beta (TRIM28), and TIF1-gamma (TRIM33), which belong to the C-VI subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a plant homeodomain (PHD), and a bromodomain (Bromo) positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TIF1 proteins couple chromatin modifications to transcriptional regulation, signaling, and tumor suppression. They exert a deacetylase-dependent silencing effect when tethered to a promoter region. TIF1alpha and TIF1beta can homodimerize and contain a PXVXL motif necessary and sufficient for heterochromatin protein 1(HP1) binding. They bind nuclear receptors and Kruppel-associated boxes (KRAB) specifically and respectively. TIF1gamma is structurally closely related to TIF1alpha and TIF1beta, but has very little functional features in common with them. It does not interact with the KRAB silencing domain of KOX1 or the heterochromatinic proteins HP1alpha, beta and gamma. It cannot bind to nuclear receptors (NRs).

                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 755503761  16 PILCPSHPAEELRLFCELCDRPVCRDCVVGEHREHPYDF 54
Cdd:cd19775    1 PLFCPVHPQEPLKLFCETCDKLTCRDCQLLEHKDHKYQF 39

B-box-type 2 zinc finger found in Drosophila melanogaster brain tumor protein (BRAT) and similar proteins; BRAT is a NHL-domain family protein that functions as a translational repressor to inhibit cell proliferation. This family also contains Caenorhabditis elegans B-box type zinc finger protein ncl-1, a C. elegans Brat homolog which functions as a translational repressor that inhibits protein synthesis. BRAT contains Bbox1 and Bbox2 zinc fingers and NHL repeats. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755503761  15 KPILCPSHPAEELRLFCELCDRPVCRDCVVGEHR--EHPYDF 54
Cdd:cd19798    2 KPVFCPKHPNEVLKFFCKTCNIPICKDCTLLDHNkgLHDYEY 43

B-box-type 2 zinc finger found in tripartite motif-containing protein TRIM2, TRIM3, and similar proteins; TRIM2, also known as RING finger protein 86 (RNF86), is an E3 ubiquitin-protein ligase that ubiquitinates the neurofilament light chain, a component of the intermediate filament in axons. Loss of function of TRIM2 results in early-onset axonal neuropathy. TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It also plays an important role in the central nervous system (CNS). In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. Both TRIM2 and TRIM3 belong to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755503761  16 PILCPSHPAEELRLFCELCDRPVCRDCVVGEHREHP 51
Cdd:cd19759    1 PLVCPNHDGETLEFYCESCETAVCRECTAGEHNEHR 36

B-box-type 2 zinc finger found in tripartite motif-containing protein 3 (TRIM3); TRIM3, also known as brain-expressed RING finger protein (BERP), RING finger protein 97 (RNF97), or RING finger protein 22 (RNF22), is an E3 ubiquitin-protein ligase involved in the pathogenesis of various cancers. It functions as a tumor suppressor that regulates asymmetric cell division in neuroblastoma. It binds to the ck inhibitor p21(WAF1/CIP1) and regulates its availability that promotes cyclins D1-cdk4 nuclear accumulation. Moreover, TRIM3 plays an important role in the central nervous system (CNS). It corresponds to gene BERP (brain-expressed RING finger protein), a unique p53-regulated gene that modulates seizure susceptibility and GABAAR cell surface expression. Furthermore, TRIM3 mediates activity-dependent turnover of presynaptic density (PSD) scaffold proteins GKAP/SAPAP1 and is a negative regulator of dendrite spine morphology. In addition, TRIM3 may be involved in vesicular trafficking via its association with the cytoskeleton-associated-recycling or transport (CART) complex that is necessary for efficient transferrin receptor recycling, but not for epidermal growth factor receptor (EGFR) degradation. It also regulates the motility of the kinesin superfamily protein KIF21B. TRIM3 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755503761  14 GKPILCPSHPAEELRLFCELCDRPVCRDCVVGEHREH 50
Cdd:cd19825    4 GKPLSCPNHEGKTMEFYCESCETAMCRECTEGEHREH 40

B-box-type 2 zinc finger (Bbox2); The B-box-type zinc finger is a short zinc binding domain of around 40 amino acid residues in length. It has been found in transcription factors, ribonucleoproteins and proto-oncoproteins, such as in TRIM (tripartite motif) proteins that consist of an N-terminal RING finger (originally called an A-box), followed by 1-2 B-box domains and a coiled-coil domain (also called RBCC for Ring, B-box, Coiled-Coil). The B-box-type zinc finger often presents in combination with other motifs, like RING zinc finger, NHL motif, coiled-coil or RFP domain in functionally unrelated proteins, most likely mediating protein-protein interaction. Based on different consensus sequence and the spacing of the 7-8 zinc-binding residues, B-box-type zinc fingers can be divided into two groups, type 1 (Bbox1: C6H2) and type 2 (Bbox2: CHC3H2). The family corresponds to type 2 B-box (Bbox2).

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755503761  18 LCPSHPAEELRLFCELCDRPVCRDCVV-GEHREHP 51
Cdd:cd19756    1 LCPEHPEEPLKLFCETCQELVCVLCLLsGEHRGHK 35

B-box-type 2 zinc finger found in tripartite motif-containing protein 71 (TRIM71) and similar proteins; TRIM71, also known as protein lineage variant 41 (lin-41), is an E3 ubiquitin-protein ligase that may play essential roles in embryonic stem cells, cellular reprogramming, and the timing of embryonic neurogenesis. It was first identified in the nematode Caenorhabditis elegans as a target of the differentiation-associated microRNA (miRNA) let-7 (lethal 7), and therefore part of a heterochronic gene network that controls larval development. In humans, it regulates let-7 microRNA biogenesis via modulation of Lin28B protein polyubiquitination. TRIM71 localizes to cytoplasmic P-bodies and directly interacts with the miRNA pathway proteins Argonaute 2 (AGO2) and DICER. It represses miRNA activity by promoting degradative ubiquitination of AGO2. Moreover, TRIM71 associates with SHCBP1, a novel component of the fibroblast growth factor (FGF) signaling pathway, and regulates its non-degradative polyubiquitination. It is also involved in the post-transcriptional regulation of the CDKN1A, RBL1 and RBL2 or EGR1 mRNAs through mediating RNA-binding in embryonic stem cells. TRIM71 belongs to the C-VII subclass of TRIM (tripartite motif)-NHL family that is defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil domain, as well as a NHL (named after proteins NCL-1, HT2A and Lin-41 that contain repeats folded into a six-bladed beta propeller) repeat domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755503761  16 PILCPSHPAEELRLFCELCDRPVCRDCVVGEHREHP 51
Cdd:cd19796    1 PSYCEIHEHEVLRLYCDTCSVPICRECTMGEHRGHS 36

B-box-type 2 zinc finger found in tripartite motif-containing protein 36 (TRIM36) and similar proteins; TRIM36, human ortholog of mouse Haprin, also known as RING finger protein 98 (RNF98) or zinc-binding protein Rbcc728, is an E3 ubiquitin-protein ligase expressed in the germ plasm. It has been implicated in acrosome reaction, fertilization, and embryogenesis, as well as in carcinogenesis. TRIM36 functions upstream of Wnt/beta-catenin activation, and plays a role in controlling the stability of proteins regulating microtubule polymerization during cortical rotation, and subsequently dorsal axis formation. It is also potentially associated with chromosome segregation through interacting with the kinetochore protein centromere protein-H (CENP-H), and colocalizing with the microtubule protein alpha-tubulin. Its overexpression may cause chromosomal instability and carcinogenesis. It is, thus, a novel regulator affecting cell cycle progression. Moreover, TRIM36 plays a critical role in the arrangement of somites during embryogenesis. TRIM36 belongs to the C-I subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as a COS (carboxyl-terminal subgroup one signature) box, a fibronectin type III (FN3) domain, and a B30.2/SPRY (SplA and ryanodine receptor) domain positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755503761  17 ILCPSHPAEELRLFCELCDRPVCRDC-VVGEHREHP 51
Cdd:cd19778    1 LMCPEHEMEKVNMYCEACRRPVCHLCkLGGSHANHR 36

B-box-type 2 zinc finger found in tripartite motif-containing protein 56 (TRIM56) and similar proteins; TRIM56, also known as RING finger protein 109 (RNF109), is a virus-inducible E3 ubiquitin ligase that restricts pestivirus infection. It positively regulates the Toll-like receptor 3 (TLR3) antiviral signaling pathway, and possesses antiviral activity against bovine viral diarrhea virus (BVDV), a ruminant pestivirus classified within the family Flaviviridae shared by tick-borne encephalitis virus (TBEV). It also possesses antiviral activity against two classical flaviviruses, yellow fever virus (YFV) and dengue virus (DENV), as well as a human coronavirus, HCoV-OC43, which is responsible for a significant share of common cold cases. It may not act on positive-strand RNA viruses indiscriminately. Moreover, TRIM56 is an interferon-inducible E3 ubiquitin ligase that modulates STING to confer double-stranded DNA-mediated innate immune responses. TRIM56 belongs to the C-V subclass of TRIM (tripartite motif) family of proteins that are defined by their N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox1 and Bbox2, and a coiled coil region, as well as an uncharacterized region positioned C-terminal to the RBCC domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 755503761  15 KPILCPSHPAEELRLFCELCDRPVCRDCVVGEHRE 49
Cdd:cd19789    1 QRIMCREHRDERLLLYCTPCEAAVCRECRLRPHLS 35

Uncharacterized protein, contains DUF3084 domain [Function unknown];

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761  64 DSVRELLRDTQPHVEALEDALAQIKSVNNALQERVEAVAADVRTFSEGY------IKAIEEHRDKLLQQLDDIRIQREtA 137
Cdd:COG4372   48 EQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELaqaqeeLESLQEEAEELQEELEELQKERQ-D 126

                         90       100
                 ....*....|....*....|...
gi 755503761 138 LQLQKAQLEQLLADMRTGVEFTE 160
Cdd:COG4372  127 LEQQRKQLEAQIAELQSEIAERE 149

Apolipoprotein A1/A4/E domain; These proteins contain several 22 residue repeats which form a pair of alpha helices. This family includes: Apolipoprotein A-I. Apolipoprotein A-IV. Apolipoprotein E.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755503761   61 KHGDSVRELLRDtqpHVEALEDALAQ-IKSVNNALQERVEAVAADVRTFSEGYIKA----IEEHRDKLLQQLDDIRIQRE 135
Cdd:pfam01442  33 KETEALRERLQK---DLEEVRAKLEPyLEELQAKLGQNVEELRQRLEPYTEELRKRlnadAEELQEKLAPYGEELRERLE 109

                          90       100
                  ....*....|....*....|....*..
gi 755503761  136 TALQLQKAQLEQLLADMRTGVEftEHL 162
Cdd:pfam01442 110 QNVDALRARLAPYAEELRQKLA--ERL 134

B-box-type 2 zinc finger found in tripartite motif-containing protein 59 (TRIM59) and similar proteins; TRIM59, also known as TRIM57, or RING finger protein 104 (RNF104) or tumor suppressor TSBF-1, is a putative E3 ubiquitin-protein ligase that functions as a novel multiple cancer biomarker for immunohistochemical detection of early tumorigenesis. It is upregulated in gastric cancer and promotes gastric carcinogenesis by interacting with and targeting the P53 tumor suppressor for its ubiquitination and degradation. It also acts as a novel accessory molecule involved in cytotoxicity of BCG-activated macrophages (BAM). Moreover, TRIM59 may serve as a multifunctional regulator for innate immune signaling pathways. It interacts with ECSIT and negatively regulates nuclear factor-kappaB (NF- kappa B) and interferon regulatory factor (IRF)-3/7-mediated signal pathways. TRIM59 belongs to the C-XI subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, Bbox2, and a coiled coil region. In addition, TRIM59 contains a C-terminal transmembrane domain.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755503761  19 CPSHPAEELRLFCELCDRPVCRDCV-VGEHREHPYD 53
Cdd:cd19790    3 CPEHYRQPLNLFCLLDRKLICGQCLtVGQHQGHPID 38

B-box-type 2 zinc finger found in tripartite motif-containing protein 14 (TRIM14) and similar proteins; TRIM14 is a mitochondrial adaptor that facilitates innate immune signaling. It also plays a critical role in tumor development. TRIM14 belongs to an unclassified TRIM (tripartite motif) family of proteins that do not have RING fingers and thus lack the characteristic tripartite (RING (R), B-box, and coiled coil (CC)) RBCC motif. It contains a Bbox2 zinc finger as well as a C-terminal SPRY/B30.2 domain. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif.

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 755503761  19 CPSHPAEELRLFCELCDRPVCRDC-VVGEHREHPYD 53
Cdd:cd19768    3 CPEHKDRPLELFCKTCKRCVCALCpILGQHRGHDVR 38